| pubmed-article:15818404 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15818404 | lifeskim:mentions | umls-concept:C0285558 | lld:lifeskim |
| pubmed-article:15818404 | lifeskim:mentions | umls-concept:C1705328 | lld:lifeskim |
| pubmed-article:15818404 | lifeskim:mentions | umls-concept:C1705341 | lld:lifeskim |
| pubmed-article:15818404 | lifeskim:mentions | umls-concept:C0108555 | lld:lifeskim |
| pubmed-article:15818404 | lifeskim:mentions | umls-concept:C0812228 | lld:lifeskim |
| pubmed-article:15818404 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15818404 | pubmed:dateCreated | 2005-5-18 | lld:pubmed |
| pubmed-article:15818404 | pubmed:abstractText | Treatment of Jurkat cells with specific inhibitors of protein kinase CK2 induces apoptosis. Here we provide evidence that the anti-apoptotic effect of CK2 can be at least partially mediated by upregulation of the Akt/PKB pathway. Such a conclusion is based on the following observations: (1) inhibition of CK2 by cell treatment with two structurally unrelated CK2 inhibitors induces downregulation of Akt/PKB, as judged from decreased phosphorylation of its physiological targets, and immunoprecipitate kinase assay; (2) similar results are observed upon reduction of CK2 catalytic subunit by the RNA-interference technique; (3) Akt/PKB Ser129 is phosphorylated by CK2 in vitro and in vivo; (4) such a phosphorylation of activated Akt/PKB correlates with a further increase in catalytic activity. These data disclose an unanticipated mechanism by which constitutive phosphorylation by CK2 may be required for maximal activation of Akt/PKB. | lld:pubmed |
| pubmed-article:15818404 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15818404 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15818404 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15818404 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15818404 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15818404 | pubmed:issn | 1350-9047 | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:ArrigoniGG | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:PinnaL ALA | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:MarinOO | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:SalviMM | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:RuzzeneMM | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:SarnoSS | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:Di MairaGG | lld:pubmed |
| pubmed-article:15818404 | pubmed:author | pubmed-author:BrustolonFF | lld:pubmed |
| pubmed-article:15818404 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15818404 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:15818404 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15818404 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15818404 | pubmed:pagination | 668-77 | lld:pubmed |
| pubmed-article:15818404 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15818404 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15818404 | pubmed:articleTitle | Protein kinase CK2 phosphorylates and upregulates Akt/PKB. | lld:pubmed |
| pubmed-article:15818404 | pubmed:affiliation | Venetian Institute of Molecular Medicine (VIMM), University of Padova, Padova, Italy. | lld:pubmed |
| pubmed-article:15818404 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15818404 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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